This Article Full Text Full Text (PDF) All Versions of this Article: 134/4/1355    most recent pp.103.033613v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (7) Citing Articles via Google Scholar Google Scholar Articles by Reinbothe, C. Articles by Reinbothe, S. Search for Related Content PubMed PubMed Citation Articles by Reinbothe, C. Articles by Reinbothe, S. Agricola Articles by Reinbothe, C. Articles by Reinbothe, S.

BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

A Novel Role of Water-Soluble Chlorophyll Proteins in the Transitory Storage of Chorophyllide^1,2

Lehrstuhl für Pflanzenphysiologie, Universität Bayreuth, D–95447 Bayreuth, Germany (C.R.); Department of Biomolecular Science, Toho University, 2–2–1 Miyama, Funabashi, Chiba 274–8510, Japan (H.S.); Université Joseph Fourier et Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5575, F–38041 Grenoble cedex 9, France (J.-P.A., S.R.); and Ruhr-Universität Bochum, Lehrstuhl für Pflanzenphysiologie, D–44801 Bochum, Germany (S.R.)

All chlorophyll (Chl)-binding proteins involved in photosynthesis of higher plants are hydrophobic membrane proteins integrated into the thylakoids. However, a different category of Chl-binding proteins, the so-called water-soluble Chl proteins (WSCPs), was found in members of the Brassicaceae, Polygonaceae, Chenopodiaceae, and Amaranthaceae families. WSCPs from different plant species bind Chl a and Chl b in different ratios. Some members of the WSCP family are induced after drought and heat stress as well as leaf detachment. It has been proposed that this group of proteins might have a physiological function in the Chl degradation pathway. We demonstrate here that a protein that shared sequence homology to WSCPs accumulated in etiolated barley (Hordeum vulgare) seedlings exposed to light for 2 h. The novel 22-kD protein was attached to the outer envelope of barley etiochloroplasts, and import of the 27-kD precursor was light dependent and induced after feeding the isolated plastids the tetrapyrrole precursor 5-aminolevulinic acid. HPLC analyses and spectroscopic pigment measurements of acetone-extracted pigments showed that the 22-kD protein is complexed with chlorophyllide. We propose a novel role of WSCPs as pigment carriers operating during light-induced chloroplast development.

² This article is dedicated to Régis Mache on the occasion of his 70^th birthday.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.033613.

^* Corresponding author; e-mail steffen.reinbothe{at}ujf-grenoble.fr; fax 0049–921–75–77–442.

Received September 19, 2003; returned for revision December 3, 2003; accepted December 3, 2003.

This article has been cited by other articles:

				M. Desclos, L. Dubousset, P. Etienne, F. Le Caherec, H. Satoh, J. Bonnefoy, A. Ourry, and J.-C. Avice A Proteomic Profiling Approach to Reveal a Novel Role of Brassica napus Drought 22 kD/Water-Soluble Chlorophyll-Binding Protein in Young Leaves during Nitrogen Remobilization Induced by Stressful Conditions Plant Physiology, August 1, 2008; 147(4): 1830 - 1844. [Abstract] [Full Text] [PDF]

				S.-Y. Park, J.-W. Yu, J.-S. Park, J. Li, S.-C. Yoo, N.-Y. Lee, S.-K. Lee, S.-W. Jeong, H. S. Seo, H.-J. Koh, et al. The Senescence-Induced Staygreen Protein Regulates Chlorophyll Degradation PLANT CELL, May 1, 2007; 19(5): 1649 - 1664. [Abstract] [Full Text] [PDF]